| Literature DB >> 3109397 |
Z Glatz, J Kovár, L Macholán, P Pec.
Abstract
Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of the homogeneous enzyme and also analysed the hydrolysed protein by several methods. The data presented here suggest that the carbonyl cofactor of diamine oxidase is firmly bound pyrroloquinoline quinone.Entities:
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Year: 1987 PMID: 3109397 PMCID: PMC1147747 DOI: 10.1042/bj2420603
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857